› 6g4p

X-ray diffraction
2.83Å resolution

Non-aged form of Torpedo californica acetylcholinesterase inhibited by tabun analog NEDPA bound to uncharged reactivator 2

Released:
DOI: 10.2210/pdb6g4p/pdb
PDB entry 6g4p coloured by chain, front view.
PDB entry 6g4p coloured by chain, side view.
PDB entry 6g4p coloured by chain, top view.
Source organism: Tetronarce californica
Primary publication:
Structure-Based Optimization of Nonquaternary Reactivators of Acetylcholinesterase Inhibited by Organophosphorus Nerve Agents.
Santoni G, de Sousa J, de la Mora E, Dias J, Jean L, Sussman JL, Silman I, Renard PY, Brown RCD, Weik M, Baati R, Nachon F
J Med Chem 61 7630-7639 (2018)
PMID: 30125110

Function and Biology Details

Reaction catalysed: 
Acetylcholine + H(2)O = choline + acetate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137375 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 537 amino acids
Theoretical weight: 60.74 KDa
Source organism: Tetronarce californica
UniProt:
  • Canonical: P04058 (Residues: 22-558; Coverage: 95%)
Gene name: ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

5 bound ligands:
Ligand NAG 4 x NAG
Ligand ELT 2 x ELT
Ligand JDS 2 x JDS
Ligand CL 8 x CL
Ligand PG4 2 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 91.51Å b: 106.56Å c: 150.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.201 0.277

Quick links

Citations

3 review citations

Organophosphorus compounds and oximes: a critical review.
Worek et al. (2020)
2 more

1 mention without citation

Structural and dynamic effects of paraoxon binding to human acetylcholinesterase by X-ray crystallography and inelastic neutron scattering.
Gerlits et al. (2022)